ID R8ASK4_PLESH Unreviewed; 926 AA.
AC R8ASK4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative zinc-dependent peptidase {ECO:0000313|EMBL:EON89306.1};
GN ORFNames=PLESHI_06172 {ECO:0000313|EMBL:EON89306.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89306.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON89306.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON89306.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EON89306.1}.
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DR EMBL; AQQO01000038; EON89306.1; -; Genomic_DNA.
DR RefSeq; WP_010862859.1; NZ_KB944507.1.
DR AlphaFoldDB; R8ASK4; -.
DR STRING; 703.SAMEA2665130_00140; -.
DR PATRIC; fig|1315976.3.peg.1215; -.
DR HOGENOM; CLU_008156_2_0_6; -.
DR Proteomes; UP000014012; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000014012};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..926
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004451437"
FT DOMAIN 45..167
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 199..371
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 674..852
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 926 AA; 103533 MW; 712EFAF12E7C37AF CRC64;
MTWLAAALML VATQVAAEAL QPDPAWLEGR LDNGLHWQIL NTPQRPNDRI ELRLLVRTGS
LQERPEQAGY AHFLEHMAFN GTARFPEQAI RDLWQQAGLT FGDDLNASTE YDNTLYRISL
PADKPQLLTP ALTWLSDVAG GLSLQPAQVS AERGVILGES LTRDKNQRSA HQQWWDYQIK
GSALAKHDPI GEAEVINSAT RERLQAFYRQ WYTPDAMTLL ISGNVDARKV SSEVAHLFAP
LQGKRSEAVP PAVLPPLAAS PLQISAHKQL NNQLLLVWDS NWQPPQDSAA LDALWLGDFV
RGLIRQRLSD AISQHGSQPI SLTLGCSVRY ARESCALSVE SDAEQRQKWL QFVATELARL
RQHGVLPSEL TLAHRLANDD LNRFYEQYAR MTSGDFINQR LFALESGAPD LGPEQYRRLR
ATFLQNLSLE RVNQELQRQL AIEPVLVLMQ PHSEAAQSAD SLMQAWRFLS AQPQAPLSRS
ESGAAAAQQM LATPAQIGQI TEQQSWPQWK LSRALLSNGL SVLVRQDPQA KDRIYLRLRS
RGGVRSLPVE LLPASQLLGV WGAHGVGPLD RTQTQQFMDV NRLDMWPLLT LSQHGLGGSS
DVEHLDAWLA MARQSLLAPK LDNQVLDDVR TQQASQLTQY LATAQGRFNQ ALDQHLFPHN
RYAELPTPAQ LKQVSLKQLQ ALHQIFISTM QDAELVVVGD VDPAKVFALA ARYLGGIDLG
GEPEWARYPF LLRQSKPLLR QDNPEDRTLV IESRLSVPAM QDDLAHRLAH DMLLRILQQR
LENQLREALG LTYGVAVDMD YPSTDMQLNL LQIRVLVAPD KQEEAQETIA EQLALLLDKG
ISEQEFTQAR GQVATSLQDI WRQPAATVEL LSQYRLAGYP LEEVMDVNQV LNGITEQTVR
DLMLHYLRAP GQLSAVFAPP VAAKSK
//